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. 2005 Aug 18;24(35):5401-13.
doi: 10.1038/sj.onc.1208714.

Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3

Chuanhai Fu  1 , Kashif Ahmed, Husheng Ding, Xia Ding, Jianping Lan, Zhihong Yang, Yong Miao, Yuanyuan Zhu, Yunyu Shi, Jingde Zhu, He Huang, Xuebiao Yao
Affiliations

Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3

Chuanhai Fu et al. Oncogene. .

Abstract

The PML gene of acute promyelocytic leukemia (APL) encodes a cell-growth and tumor suppressor. PML localizes to discrete nuclear bodies (NBs) that are disrupted in APL cells, resulting from a reciprocal chromosome translocation t (15;17). Here we show that the nuclear localization of PML is also regulated by SUMO-3, one of the three recently identified SUMO isoforms in human cells. SUMO-3 bears similar subcellular distribution to those of SUMO-1 and -2 in the interphase nuclear body, which is colocalized with PML protein. However, both SUMO-2 and -3 are also localized to nucleoli, a region lacking SUMO-1. Immunoprecipitated PML protein bears SUMO-3 moiety in a covalently modified form, supporting the notion that PML is conjugated by SUMO-3. To determine the functional relevance of SUMO-3 conjugation on PML molecular dynamics, we suppressed SUMO-3 protein expression using a siRNA-mediated approach. Depletion of SUMO-3 markedly reduced the number of PML-containing NBa and their integrity, which is rescued by exogenous expression of SUMO-3 but not SUMO-1 or SUMO-2. The specific requirement of SUMO-3 for PML nuclear localization is validated by expression of SUMO-3 conjugation defective mutant. Moreover, we demonstrate that oligomerization of SUMO-3 is required for PML retention in the nucleus. Taken together, our studies provide first line of evidence showing that SUMO-3 is essential for PML localization and offer novel insight into the pathobiochemistry of APL.

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